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XB-ART-18748
Cell Biol Int 1996 Jan 01;201:67-72. doi: 10.1006/cbir.1996.0010.
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Structure-function relationships of Na+/K(+)-pumps expressed in Xenopus oocytes.

Schwarz W , Vasilets LA .


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During the last years we have examined structure-function relationships in the Na+/K(+)-ATPase with respect to interactions of the external cations with the pump molecule. We have analysed in voltage-clamp experiments the influence of extracellular Na+ and K+ on the current generated by Na+/K(+)-pumps expressed in Xenopus oocytes. Our results demonstrated that external Na+ and K+ have to pass an access channel in the electrical field of the membrane to reach their binding sites. This external access, therefore, is voltage-dependent and is affected by lysine residues within the cytoplasmic N-terminus, by glutamic acid residues in intramembraneous domains, the ouabain sensitivity and phosphorylation by protein kinases.

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